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Biomedical subjects

L S Mil'man

Publications and source records attributed to L S Mil'man.

At least 37 records · Page 2Linked to original sources
PubMedDate not supplied

[The isoenzyme composition of liver pyruvate kinase from hens in ontogeny].

Only one isozyme M2 of pyruvate kinase was found in the liver of hens at all stages of embryonic and postembryonic development. No analogue to isozyme L from the liver of mammals was found. During embryogenesis and postnatal life, isozyme M2 is presented by two forms which differ in pI values. Throughout embryonic and postembryonic development, pyruvate kinase is presented by two forms which differ in their substrate affinity.

Animals↗
PubMedDate not supplied

[The key enzymes of the alternative pathways of serine utilization in gluconeogenesis in chickens during individual development].

It has been shown that in embryonic liver and kidney of chicks, serine is involved into gluconeogenesis almost exclusively via serine-pyruvate aminotransferase. This relationship stands true also for the liver of adult hens. On the contrary, in the kidney of adult hens, there is a significant increase in the activity of serine dehydratase, as compared to the level of the activity of this enzyme in embryogenesis and in the liver of adult hens.

Animals↗
PubMedDate not supplied

[The enzymes of fructose metabolism in the liver of chick embryos].

The activity of fructose cycle enzymes remains practically constant in chick embryonic liver during ontogenesis. Change in ratio of aldolase A to B activities was detected. It is suggested that fructose enters the cycle via the sorbitol pathway in which aldose reductase and sorbitol dehydrogenase are involved.

Aging↗
PubMedDate not supplied

[Supramolecular organization of glycolytic enzymes].

On the basis of the analysis of the data on adsorption of glycolytic enzymes to structural proteins of skeletal muscle and to erythrocyte membranes, the data on enzyme-enzyme interactions and the data on the regulation of activity of glycolytic enzymes by cellular metabolites the structure of glycolytic enzyme complex adsorbed to a biological support has been proposed. The key role in the formation of the multienzyme complex belongs to 6-phosphofructokinase. The enzyme molecule has two association sites, one of which provides the fixation of 6-phosphofructokinase on the support and another is saturated by fructose-1,6-bisphosphate aldolase. The multienzyme complex fixed on structural proteins of skeletal muscle contains one tetrameric molecule of 6-phosphofructokinase and at two molecules of other glycolytic enzymes. Hexokinase is not involved in the complex composition. The molecular mass of the multienzyme complex is about 2,6 X 10(6) Da. The formation of the multienzyme complex leads to the compartmentation of the glycolytic process. The problem of integration of physico-chemical mechanisms of enzyme activity regulation (allosteric, dissociative and adsorptive mechanisms) is discussed.

Animals↗